Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.
KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-de...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2014
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| _version_ | 1797085267732987904 |
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| author | Zubcevic, L Bavro, V Muniz, JR Schmidt, MR Wang, S De Zorzi, R Venien-Bryan, C Sansom, MS Nichols, C Tucker, S |
| author_facet | Zubcevic, L Bavro, V Muniz, JR Schmidt, MR Wang, S De Zorzi, R Venien-Bryan, C Sansom, MS Nichols, C Tucker, S |
| author_sort | Zubcevic, L |
| collection | OXFORD |
| description | KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating. |
| first_indexed | 2024-03-07T02:06:29Z |
| format | Journal article |
| id | oxford-uuid:9f2e0838-9104-4691-8382-a6f88ca266d5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:06:29Z |
| publishDate | 2014 |
| record_format | dspace |
| spelling | oxford-uuid:9f2e0838-9104-4691-8382-a6f88ca266d52022-03-27T00:55:28ZControl of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9f2e0838-9104-4691-8382-a6f88ca266d5EnglishSymplectic Elements at Oxford2014Zubcevic, LBavro, VMuniz, JRSchmidt, MRWang, SDe Zorzi, RVenien-Bryan, CSansom, MSNichols, CTucker, SKirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating. |
| spellingShingle | Zubcevic, L Bavro, V Muniz, JR Schmidt, MR Wang, S De Zorzi, R Venien-Bryan, C Sansom, MS Nichols, C Tucker, S Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. |
| title | Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. |
| title_full | Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. |
| title_fullStr | Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. |
| title_full_unstemmed | Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. |
| title_short | Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. |
| title_sort | control of kirbac3 1 potassium channel gating at the interface between cytoplasmic domains |
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